Ontology highlight
ABSTRACT:
SUBMITTER: Duez C
PROVIDER: S-EPMC95044 | biostudies-literature | 2001 Mar
REPOSITORIES: biostudies-literature
Duez C C Vanhove M M Gallet X X Bouillenne F F Docquier J J Brans A A Frère J J
Journal of bacteriology 20010301 5
Penicillin-binding protein 4a (PBP4a) from Bacillus subtilis was overproduced and purified to homogeneity. It clearly exhibits DD-carboxypeptidase and thiolesterase activities in vitro. Although highly isologous to the Actinomadura sp. strain R39 DD-peptidase (B. Granier, C. Duez, S. Lepage, S. Englebert, J. Dusart, O. Dideberg, J. van Beeumen, J. M. Frère, and J. M. Ghuysen, Biochem. J. 282:781-788, 1992), which is rapidly inactivated by many beta-lactams, PBP4a is only moderately sensitive to ...[more]